6H5N
Plasmodium falciparum Pfs48/45 C-terminal domain bound to monoclonal antibody 85RF45.1
Summary for 6H5N
| Entry DOI | 10.2210/pdb6h5n/pdb |
| Descriptor | Gametocyte surface protein P45/48, Antibody 85RF45.1 light chain, Antibody 85RF45.1 heavy chain (3 entities in total) |
| Functional Keywords | pfs48/45 gamete fusion plasmodium falciparum transmission blocking monoclonal antibody, cell invasion |
| Biological source | Plasmodium falciparum (isolate 3D7) More |
| Total number of polymer chains | 6 |
| Total formula weight | 124270.55 |
| Authors | Lennartz, F.,Higgins, M.K. (deposition date: 2018-07-25, release date: 2018-09-26, Last modification date: 2024-11-13) |
| Primary citation | Lennartz, F.,Brod, F.,Dabbs, R.,Miura, K.,Mekhaiel, D.,Marini, A.,Jore, M.M.,Sogaard, M.M.,Jorgensen, T.,de Jongh, W.A.,Sauerwein, R.W.,Long, C.A.,Biswas, S.,Higgins, M.K. Structural basis for recognition of the malaria vaccine candidate Pfs48/45 by a transmission blocking antibody. Nat Commun, 9:3822-3822, 2018 Cited by PubMed Abstract: The quest to develop an effective malaria vaccine remains a major priority in the fight against global infectious disease. An approach with great potential is a transmission-blocking vaccine which induces antibodies that prevent establishment of a productive infection in mosquitos that feed on infected humans, thereby stopping the transmission cycle. One of the most promising targets for such a vaccine is the gamete surface protein, Pfs48/45. Here we establish a system for production of full-length Pfs48/45 and use this to raise a panel of monoclonal antibodies. We map the binding regions of these antibodies on Pfs48/45 and correlate the location of their epitopes with their transmission-blocking activity. Finally, we present the structure of the C-terminal domain of Pfs48/45 bound to the most potent transmission-blocking antibody, and provide key molecular information for future structure-guided immunogen design. PubMed: 30237518DOI: 10.1038/s41467-018-06340-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.23 Å) |
Structure validation
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